2xxs

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[[Image:2xxs.png|left|200px]]
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==SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE SHIGELLA TYPE III SECRETION PROTEIN MXIG==
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<StructureSection load='2xxs' size='340' side='right' caption='[[2xxs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xxs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXS OCA]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xxs RCSB], [http://www.ebi.ac.uk/pdbsum/2xxs PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MxiG is a single-pass membrane protein that oligomerizes within the inner membrane ring of the Shigella flexneri type III secretion system (T3SS). The MxiG N-terminal domain (MxiG-N) is the predominant cytoplasmic structure; however, its role in T3SS assembly and secretion is largely uncharacterized. We have determined the solution structure of MxiG-N residues 6-112 (MxiG-N(6-112)), representing the first published structure of this T3SS domain. The structure shows strong structural homology to forkhead-associated (FHA) domains. Canonically, these cell-signaling modules bind phosphothreonine (Thr(P)) via highly conserved residues. However, the putative phosphate-binding pocket of MxiG-N(6-112) does not align with other FHA domain structures or interact with Thr(P). Furthermore, mutagenesis of potential phosphate-binding residues has no effect on S. flexneri T3SS assembly and function. Therefore, MxiG-N has a novel function for an FHA domain. Positioning of MxiG-N(6-112) within the EM density of the S. flexneri needle complex gives insight into the ambiguous stoichiometry of the T3SS, supporting models with 24 MxiG subunits in the inner membrane ring.
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Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG.,McDowell MA, Johnson S, Deane JE, Cheung M, Roehrich AD, Blocker AJ, McDonnell JM, Lea SM J Biol Chem. 2011 Sep 2;286(35):30606-14. Epub 2011 Jul 5. PMID:21733840<ref>PMID:21733840</ref>
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The line below this paragraph, containing "STRUCTURE_2xxs", creates the "Structure Box" on the page.
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{{STRUCTURE_2xxs| PDB=2xxs | SCENE= }}
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===SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE SHIGELLA TYPE III SECRETION PROTEIN MXIG===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21733840}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 21733840 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21733840}}
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==About this Structure==
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[[2xxs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXS OCA].
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==Reference==
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<ref group="xtra">PMID:021733840</ref><references group="xtra"/>
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[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
[[Category: Deane, J E.]]
[[Category: Deane, J E.]]

Revision as of 07:45, 14 May 2014

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE SHIGELLA TYPE III SECRETION PROTEIN MXIG

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